To be disordered or not to be disordered: is that still a question for proteins in the cell?
Cell Mol Life Sci
; 74(17): 3185-3204, 2017 09.
Article
em En
| MEDLINE
| ID: mdl-28612216
ABSTRACT
There is ample evidence that many proteins or regions of proteins lack a well-defined folded structure under native-like conditions. These are called intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). Whether this intrinsic disorder is also their main structural characteristic in living cells has been a matter of intense debate. The structural analysis of IDPs became an important challenge also because of their involvement in a plethora of human diseases, which made IDPs attractive targets for therapeutic development. Therefore, biophysical approaches are increasingly being employed to probe the structural and dynamical state of proteins, not only in isolation in a test tube, but also in a complex biological environment and even within intact cells. Here, we survey direct and indirect evidence that structural disorder is in fact the physiological state of many proteins in the proteome. The paradigmatic case of α-synuclein is used to illustrate the controversial nature of this topic.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Intrinsicamente Desordenadas
Limite:
Humans
Idioma:
En
Revista:
Cell Mol Life Sci
Ano de publicação:
2017
Tipo de documento:
Article